Inhibition of beta-amyloid aggregation by fluorescent dye labels

Mariana Amaro, Thorben Wellbrock, David Birch, Olaf Rolinski

Research output: Contribution to journalLetter

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Abstract

The fluorescence decay of beta-amyloid’s (Ab) intrinsic fluorophore tyrosine has been used for sensing the oligomer formation of dye-labelled Ab monomers and the results compared with previously studied oligomerization of the non-labelled Ab peptides. It has been demonstrated that two different sized, covalently bound probes 7-diethylaminocoumarin-3-carbonyl and Hilyte Fluor 488 (HLF), alter the rate and character of oligomerization to different extents. The ability of HLF to inhibit formation of highly ordered structures containing beta-sheets was also shown. The implications of our findings for using fluorescence methods in amyloidosis research are discussed and the advantages of this auto-fluorescence approach highlighted.
Original languageEnglish
Article number063704
Number of pages5
JournalApplied Physics Letters
Volume104
Issue number6
Early online date12 Feb 2014
DOIs
Publication statusPublished - 12 Feb 2014

Keywords

  • aggregation
  • fluorescent dye labels
  • peptides

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